SMOX: Difference between revisions

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{{Infobox_gene}}
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'''Spermine oxidase''' is an [[enzyme]] that in humans is encoded by the ''SMOX'' [[gene]].<ref name="pmid11454677">{{cite journal | vauthors = Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA | title = Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure | journal = Cancer Research | volume = 61 | issue = 14 | pages = 5370–3 | date = July 2001 | pmid = 11454677 | pmc =  | doi =  }}</ref><ref name="pmid12398765">{{cite journal | vauthors = Murray-Stewart T, Wang Y, Devereux W, Casero RA | title = Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics | journal = The Biochemical Journal | volume = 368 | issue = Pt 3 | pages = 673–7 | date = December 2002 | pmid = 12398765 | pmc = 1223052 | doi = 10.1042/BJ20021587 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SMOX spermine oxidase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54498| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Spermine oxidase
| HGNCid = 15862
| Symbol = SMOX
| AltSymbols =; SMO; C20orf16; FLJ20746; MGC1010; PAO; PAOh1; dJ779E11.1
| OMIM = 
| ECnumber = 
| Homologene = 69268
| MGIid = 2445356
| GeneAtlas_image1 = PBB_GE_SMOX_210357_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMOX_217074_at_tn.png
| Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046592 |text = polyamine oxidase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0046208 |text = spermine catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 54498
    | Hs_Ensembl = ENSG00000088826
    | Hs_RefseqProtein = NP_787033
    | Hs_RefseqmRNA = NM_175839
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 4077450
    | Hs_GenLoc_end = 4116369
    | Hs_Uniprot = Q9NWM0
    | Mm_EntrezGene = 228608
    | Mm_Ensembl = ENSMUSG00000027333
    | Mm_RefseqmRNA = NM_145533
    | Mm_RefseqProtein = NP_663508
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 131183384
    | Mm_GenLoc_end = 131216613
    | Mm_Uniprot = Q3UPW5
  }}
}}
'''Spermine oxidase''', also known as '''SMOX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SMOX spermine oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54498| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The product of this gene is the [[polyamine oxidase]]. This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The product of this gene is the polyamine oxidase. This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.<ref name="entrez">{{cite web | title = Entrez Gene: SMOX spermine oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54498| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Seiler N | title = Catabolism of polyamines | journal = Amino Acids | volume = 26 | issue = 3 | pages = 217–33 | date = June 2004 | pmid = 15221502 | doi = 10.1007/s00726-004-0070-z }}
| citations =
* {{cite journal | vauthors = Hölttä E | title = Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase | journal = Biochemistry | volume = 16 | issue = 1 | pages = 91–100 | date = January 1977 | pmid = 12798 | doi = 10.1021/bi00620a015 }}
*{{cite journal | author=Seiler N |title=Catabolism of polyamines. |journal=Amino Acids |volume=26 |issue= 3 |pages= 217-33 |year= 2005 |pmid= 15221502 |doi= 10.1007/s00726-004-0070-z }}
* {{cite journal | vauthors = Tsukada T, Furusako S, Maekawa S, Hibasami H, Nakashima K | title = Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase | journal = The International Journal of Biochemistry | volume = 20 | issue = 7 | pages = 695–702 | year = 1988 | pmid = 3181599 | doi = 10.1016/0020-711X(88)90164-4 }}
*{{cite journal | author=Hölttä E |title=Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. |journal=Biochemistry |volume=16 |issue= 1 |pages= 91-100 |year= 1977 |pmid= 12798 |doi= }}
* {{cite journal | vauthors = Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW | title = Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin | journal = The Biochemical Journal | volume = 367 | issue = Pt 3 | pages = 665–75 | date = November 2002 | pmid = 12141946 | pmc = 1222929 | doi = 10.1042/BJ20020720 }}
*{{cite journal | author=Tsukada T, Furusako S, Maekawa S, ''et al.'' |title=Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase. |journal=Int. J. Biochem. |volume=20 |issue= 7 |pages= 695-702 |year= 1988 |pmid= 3181599 |doi= }}
* {{cite journal | vauthors = Cervelli M, Polticelli F, Federico R, Mariottini P | title = Heterologous expression and characterization of mouse spermine oxidase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 7 | pages = 5271–6 | date = February 2003 | pmid = 12458219 | doi = 10.1074/jbc.M207888200 }}
*{{cite journal  | author=Wang Y, Devereux W, Woster PM, ''et al.'' |title=Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. |journal=Cancer Res. |volume=61 |issue= 14 |pages= 5370-3 |year= 2001 |pmid= 11454677 |doi=  }}
* {{cite journal | vauthors = Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA | title = Properties of purified recombinant human polyamine oxidase, PAOh1/SMO | journal = Biochemical and Biophysical Research Communications | volume = 304 | issue = 4 | pages = 605–11 | date = May 2003 | pmid = 12727196 | doi = 10.1016/S0006-291X(03)00636-3 }}
*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
* {{cite journal | vauthors = Cervelli M, Bellini A, Bianchi M, Marcocci L, Nocera S, Polticelli F, Federico R, Amendola R, Mariottini P | title = Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform | journal = European Journal of Biochemistry | volume = 271 | issue = 4 | pages = 760–70 | date = February 2004 | pmid = 14764092 | doi = 10.1111/j.1432-1033.2004.03979.x }}
*{{cite journal | author=Vujcic S, Diegelman P, Bacchi CJ, ''et al.'' |title=Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. |journal=Biochem. J. |volume=367 |issue= Pt 3 |pages= 665-75 |year= 2002 |pmid= 12141946 |doi= 10.1042/BJ20020720 }}
* {{cite journal | vauthors = Pledgie A, Huang Y, Hacker A, Zhang Z, Woster PM, Davidson NE, Casero RA | title = Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines | journal = The Journal of Biological Chemistry | volume = 280 | issue = 48 | pages = 39843–51 | date = December 2005 | pmid = 16207710 | doi = 10.1074/jbc.M508177200 }}
*{{cite journal  | author=Murray-Stewart T, Wang Y, Devereux W, Casero RA |title=Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics. |journal=Biochem. J. |volume=368 |issue= Pt 3 |pages= 673-7 |year= 2003 |pmid= 12398765 |doi= 10.1042/BJ20021587 }}
*{{cite journal | author=Cervelli M, Polticelli F, Federico R, Mariottini P |title=Heterologous expression and characterization of mouse spermine oxidase. |journal=J. Biol. Chem. |volume=278 |issue= 7 |pages= 5271-6 |year= 2003 |pmid= 12458219 |doi= 10.1074/jbc.M207888200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Wang Y, Murray-Stewart T, Devereux W, ''et al.'' |title=Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. |journal=Biochem. Biophys. Res. Commun. |volume=304 |issue= 4 |pages= 605-11 |year= 2003 |pmid= 12727196 |doi=  }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Cervelli M, Bellini A, Bianchi M, ''et al.'' |title=Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform. |journal=Eur. J. Biochem. |volume=271 |issue= 4 |pages= 760-70 |year= 2004 |pmid= 14764092 |doi= }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Pledgie A, Huang Y, Hacker A, ''et al.'' |title=Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines. |journal=J. Biol. Chem. |volume=280 |issue= 48 |pages= 39843-51 |year= 2006 |pmid= 16207710 |doi= 10.1074/jbc.M508177200 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 06:41, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

n/a

RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Spermine oxidase is an enzyme that in humans is encoded by the SMOX gene.[1][2][3]

Function

The product of this gene is the polyamine oxidase. This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.[3]

References

  1. ↑ Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA (July 2001). "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure". Cancer Research. 61 (14): 5370–3. PMID 11454677.
  2. ↑ Murray-Stewart T, Wang Y, Devereux W, Casero RA (December 2002). "Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics". The Biochemical Journal. 368 (Pt 3): 673–7. doi:10.1042/BJ20021587. PMC 1223052. PMID 12398765.
  3. ↑ 3.0 3.1 "Entrez Gene: SMOX spermine oxidase".

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=SMOX&oldid=1419590"